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Updated: Jan 23, 2026

Assessment of Open Probability of the Mitochondrial Permeability Transition Pore in the Setting of Coenzyme Q Excess
Published on: June 1, 2022
F-ATP synthase and the permeability transition pore: fewer doubts, more certainties
Michela Carraro1, Vanessa Checchetto2, Ildikó Szabó2
1Department of Biomedical Sciences, University of Padova, Italy.
Abstract:
Whether the mitochondrial permeability transition pore (PTP), also called mitochondrial megachannel (MMC), originates from the F-ATP synthase is a matter of controversy. This hypothesis is supported both by site-directed mutagenesis of specific residues of F-ATP synthase affecting regulation of the PTP/MMC and by deletion of specific subunits causing dramatic changes in channel conductance. In contrast, human cells lacking an assembled F-ATP synthase apparently display persistence of the PTP. We discuss recent data that shed new light on this controversy, supporting the conclusion that the PTP/MMC originates from a Ca2+ -dependent conformational change in F-ATP synthase allowing its reversible transformation into a high-conductance channel.
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